Study on the interaction of ethylene glycol with trypsin: Binding ability, activity, and stability

L Momeni, S Farhadian, B Shareghi - Journal of Molecular Liquids, 2022 - Elsevier
The study of the structural changes and thermal stabilities of proteins in the presence of
various co-solutes is a critical element of basic research, drug discovery, and development …

Interaction of polyethylene glycol with cytochrome c investigated via in vitro and in silico approaches

ZA Parray, F Ahmad, MF Alajmi, A Hussain… - Scientific reports, 2021 - nature.com
One of the significant proteins that have attracted research groups due to virtue of being a
potent selective anticancer drug target and property of triggering apoptosis upon release in …

Heparin accelerates the protein aggregation via the downhill polymerization mechanism: multi-spectroscopic studies to delineate the implications on proteinopathies

IA Ahanger, ZA Parray, K Nasreen, F Ahmad… - ACS …, 2021 - ACS Publications
Heparin is one of the members of the glycosaminoglycan (GAG) family, which has been
associated with protein aggregation diseases including Alzheimer's disease, Parkinson's …

Size-Dependent Interplay of Volume Exclusion Versus Soft Interactions: Cytochrome c in Macromolecular Crowded Environment

ZA Parray, F Ahmad, AA Chaudhary… - Frontiers in molecular …, 2022 - frontiersin.org
Even though there are a great number of possible conformational states, how a protein
generated as a linear unfolded polypeptide efficiently folds into its physiologically active …

Measuring Structural Changes in Cytochrome c under Crowded Conditions Using In Vitro and In Silico Approaches

ZA Parray, AAT Naqvi, IA Ahanger, M Shahid, F Ahmad… - Polymers, 2022 - mdpi.com
It is known from in vitro studies that macromolecular crowding in the cell effects protein
structure, stability and function; but predictive studies are relatively unexplored. There are …

[HTML][HTML] Structural refolding and thermal stability of myoglobin in the presence of mixture of crowders: importance of various interactions for protein stabilization in …

ZA Parray, F Ahmad, MI Hassan, A Ahmed… - Molecules, 2021 - mdpi.com
The intracellular environment is overcrowded with a range of molecules (small and large),
all of which influence protein conformation. As a result, understanding how proteins fold and …

Temperature-dependent dynamics at protein–solvent interfaces

M Reuhl, M Vogel - The Journal of Chemical Physics, 2022 - pubs.aip.org
We perform differential scanning calorimetry, broadband dielectric spectroscopy (BDS), and
nuclear magnetic resonance (NMR) studies to understand the molecular dynamics in …

Interaction studies of recombinant laccase with co-solutes: Using various spectroscopic, calorimetric, and in silico approaches

ZA Parray, A Hamza, P Bhardwaj, A Samad… - Journal of Molecular …, 2023 - Elsevier
The co-solute engineering is a rational approach to elucidate protein-molecule interactions
which involves an exhaustive understanding of the structural characteristics of active sites of …

Characterization of different intermediate states in myoglobin induced by polyethylene glycol: A process of spontaneous molecular self-organization foresees the …

ZA Parray, AAT Naqvi, F Ahmad, MI Hassan… - Journal of Molecular …, 2021 - Elsevier
Practically proteins perform their functions exposed to various molecules (macro/micro) of
different shapes, sizes, and high concentrations. In such conditions, proteins fold through …

Thermal properties of glycinin in crowded environments

K Ni, A Liu, Y Ding, X Ye - International Journal of Biological …, 2024 - Elsevier
Crowded environments, commonly found in the food system, are utilized to enhance the
properties of soybean proteins. Despite their widespread application, little information exists …